pubmed-article:1408764 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1408764 | lifeskim:mentions | umls-concept:C0014139 | lld:lifeskim |
pubmed-article:1408764 | lifeskim:mentions | umls-concept:C0085104 | lld:lifeskim |
pubmed-article:1408764 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:1408764 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
pubmed-article:1408764 | lifeskim:mentions | umls-concept:C0301869 | lld:lifeskim |
pubmed-article:1408764 | pubmed:issue | 17 | lld:pubmed |
pubmed-article:1408764 | pubmed:dateCreated | 1992-10-30 | lld:pubmed |
pubmed-article:1408764 | pubmed:abstractText | Inhibition of gene expression by antisense oligonucleotides is limited by their low ability to enter cells. Knowing that sugar binding receptors, also called membrane lectins, efficiently internalize neoglycoproteins bearing the relevant sugar, 6-phosphomannose, for instance, oligonucleotides--substituted on their 5'-end with either a fluorescent probe or a radioactive label on the one hand, and bearing a thiol function on their 3'-end, on the other hand,--were coupled onto 6-phosphomannosylated proteins via a disulfide bridge. The oligonucleotide bound to 6-phosphomannosylated serum albumin is much more efficiently internalized roughly 20 times than the free oligonucleotide. Although most of the oligonucleotides are associated with vesicular compartments, oligonucleotides after releasing from the carrier by reduction of the disulfide bridge may find their way to reach the cytosol and then lead to an increase in the efficiency of the oligonucleotides. | lld:pubmed |
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pubmed-article:1408764 | pubmed:language | eng | lld:pubmed |
pubmed-article:1408764 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1408764 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1408764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1408764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:1408764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1408764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1408764 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1408764 | pubmed:month | Sep | lld:pubmed |
pubmed-article:1408764 | pubmed:issn | 0305-1048 | lld:pubmed |
pubmed-article:1408764 | pubmed:author | pubmed-author:MonsignyMM | lld:pubmed |
pubmed-article:1408764 | pubmed:author | pubmed-author:RocheA CAC | lld:pubmed |
pubmed-article:1408764 | pubmed:author | pubmed-author:ThuongN TNT | lld:pubmed |
pubmed-article:1408764 | pubmed:author | pubmed-author:MidouxPP | lld:pubmed |
pubmed-article:1408764 | pubmed:author | pubmed-author:BonfilsEE | lld:pubmed |
pubmed-article:1408764 | pubmed:author | pubmed-author:DepierreuxCC | lld:pubmed |
pubmed-article:1408764 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1408764 | pubmed:day | 11 | lld:pubmed |
pubmed-article:1408764 | pubmed:volume | 20 | lld:pubmed |
pubmed-article:1408764 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1408764 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1408764 | pubmed:pagination | 4621-9 | lld:pubmed |
pubmed-article:1408764 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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